Currently we are investigating the feasibility of using hen egg white lysozyme as a model protein for studying two-state and non-two-state protein denaturation, induced with heat or with strong denaturants, by varying the pH. We are carrying out preliminary experiments monitoring the thermally induced unfolding of lysozyme as a function of pH by means of protein difference spectra and second derivative spectra with a photodiode array spectrophotometer. With an appropriate model system, eventually we plan to investigate protein unfolding/refolding by equilibrium and kinetic techniques under two-state and non-two-state conditions while utilizing various denaturing agents in an effort to understand different folding pathways.